Biochemical characterization of a 34 kda ribonucleoprotein (p34) purified from the spinach chloroplast fraction as an effective phosphate acceptor for casein kinase II-Reference-Cited by-同舟云学术

Biochemical characterization of a 34 kda ribonucleoprotein (p34) purified from the spinach chloroplast fraction as an effective phosphate acceptor for casein kinase II

Published:1993-12-06 Issue:2 Volume:335 Page:176-180
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:

Author:

Kanekatsu Motoki,Munakata Hiroshi,Furuzono Kazuhisa,Ohtsuki Kenzo

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(93)80724-9/fullpdf

Reference17 articles.

1. Casein kinase 2: An ‘eminence grise’ in cellular regulation?

2. Casein kinase II phosphorylates the eukaryote-specific C-terminal domain of topoisomerase II in vivo.

3. The replication functions of SV40 T antigen are regulated by phosphorylation

4. The in vitro replication of DNA containing the SV40 origin.

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3. Identification and characterization of chloroplast casein kinase II from Oryza sativa (rice);Journal of Experimental Botany;2014-10-14

4. The Peptide Microarray “ChloroPhos1.0” Identifies New Phosphorylation Targets of Plastid Casein Kinase II (pCKII) in Arabidopsis thaliana;PLoS ONE;2014-10-08

5. Chloroplast Gene Expression—RNA Synthesis and Processing;Plastid Biology;2014